Recombinant Human AKTIP Protein, GST-tagged
Cat.No. : | AKTIP-4535H |
Product Overview : | Human FTS full-length ORF ( AAH01134, 1 a.a. - 292 a.a.) recombinant protein with GST-tag at N-terminal. |
- Specification
- Gene Information
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Description : | The mouse homolog of this gene produces fused toes and thymic hyperplasia in heterozygous mutant animals while homozygous mutants die in early development. This gene may play a role in apoptosis as these morphological abnormalities are caused by altered patterns of programmed cell death. The protein encoded by this gene is similar to the ubiquitin ligase domain of other ubiquitin-conjugating enzymes but lacks the conserved cysteine residue that enables those enzymes to conjugate ubiquitin to the target protein. This protein interacts directly with serine/threonine kinase protein kinase B (PKB)/Akt and modulates PKB activity by enhancing the phosphorylation of PKBs regulatory sites. Alternative splicing results in two transcript variants encoding the same protein. [provided by RefSeq |
Source : | Wheat Germ |
Species : | Human |
Tag : | GST |
Molecular Mass : | 57.86 kDa |
AA Sequence : | MNPFWSMSTSSVRKRSEGEEKTLTG DVKTSPPRTAPKKQLPSIPKNALPI TKPTSPAPAAQSTNGTHASYGPFYL EYSLLAEFTLVVKQKLPGVYVQPSY RSALMWFGVIFIRHGLYQDGVFKFT VYIPDNYPDGDCPRLVFDIPVFHPL VDPTSGELDVKRAFAKWRRNHNHIW QVLMYARRVFYKIDTASPLNPEAAV LYEKDIQLFKSKVVDSVKVCTARLF DQPKIEDPYAISFSPWNPSVHDEAR EKMLTQKKPEEQHNKSVHVAGLSWV KPGSVQPFSKEEKTVAT |
Applications : | Enzyme-linked Immunoabsorbent Assay Western Blot (Recombinant protein) Antibody Production Protein Array |
Notes : | Best use within three months from the date of receipt of this protein. |
Storage : | Store at -80 centigrade. Aliquot to avoid repeated freezing and thawing. |
Storage Buffer : | 50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer. |
Gene Name : | AKTIP AKT interacting protein [ Homo sapiens ] |
Official Symbol : | AKTIP |
Synonyms : | AKTIP; AKT interacting protein; FTS, fused toes (mouse) homolog, fused toes homolog (mouse); AKT-interacting protein; FLJ13258; fused toes homolog; fused toes protein homolog; FT1; FTS; |
Gene ID : | 64400 |
mRNA Refseq : | NM_001012398 |
Protein Refseq : | NP_001012398 |
MIM : | 608483 |
UniProt ID : | Q9H8T0 |
Products Types
◆ Recombinant Protein | ||
AKTIP-264R | Recombinant Rat AKTIP Protein, His (Fc)-Avi-tagged | +Inquiry |
AKTIP-41C | Recombinant Cynomolgus Monkey AKTIP Protein, His (Fc)-Avi-tagged | +Inquiry |
AKTIP-445M | Recombinant Mouse AKTIP Protein, His (Fc)-Avi-tagged | +Inquiry |
Aktip-1587M | Recombinant Mouse Aktip Protein, Myc/DDK-tagged | +Inquiry |
AKTIP-4783H | Recombinant Human AKTIP protein, His-SUMO-tagged | +Inquiry |
◆ Lysates | ||
AKTIP-8926HCL | Recombinant Human AKTIP 293 Cell Lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (12)
Ask a questionThe structural features of AKTIP protein have not been extensively characterized. AKTIP contains multiple domains, including an N-terminal pleckstrin homology (PH) domain and a C-terminal coiled-coil domain. The PH domain is known to interact with phospholipids, suggesting a potential role for AKTIP in membrane association. The coiled-coil domain may be involved in protein-protein interactions and the formation of protein complexes.
Information on genetic variations or mutations in the AKTIP gene is limited. However, genetic variations in AKTIP could potentially exist and contribute to the development of specific diseases. Further research and genetic studies are necessary to investigate potential genetic variations or mutations in the AKTIP gene and their associations with diseases or phenotypic traits.
Currently, there have been no specific inhibitors or activators developed for AKTIP protein. However, targeting AKT, the protein that interacts with AKTIP, has been the focus of drug development in various diseases. Small molecule inhibitors of AKT kinase activity, such as MK-2206 and AZD5363, have been developed and are being evaluated in clinical trials. It's possible that targeting AKT could indirectly affect AKTIP function, but direct modulation of AKTIP itself will require further research and development.
Targeting AKTIP protein or its interaction with AKT could have therapeutic implications in diseases where dysregulation of AKT signaling is involved. Modulating AKTIP's function could potentially impact AKT activity and cellular processes regulated by AKT, such as cell growth, survival, and metabolism. However, further research is needed to fully understand the therapeutic potential and feasibility of targeting AKTIP for intervention or drug development.
AKTIP primarily interacts with and regulates AKT signaling. However, some studies suggest that AKTIP may also interact with other signaling molecules and pathways. For instance, AKTIP has been found to interact with phosphoinositide 3-kinase (PI3K) and contribute to PI3K-dependent signaling. Additionally, AKTIP has been reported to interact with Src kinase and play a role in Src-mediated signaling. Further investigation is needed to determine the extent of AKTIP's involvement in other signaling pathways.
The expression of AKTIP protein is not well-documented in all tissues. However, studies have reported its expression in various tissues, including the heart, brain, liver, kidney, muscle, and immune cells. Different tissues may have different expression levels of AKTIP, and its expression may be regulated in a tissue-specific manner.
AKTIP interacts with several proteins involved in AKT signaling and other cellular processes. Some of the known interactions include binding to AKT isoforms (AKT1, AKT2, AKT3) and modulating their activity and localization. AKTIP also interacts with other signaling molecules such as PI3K (phosphoinositide 3-kinase) and PHLPP (PH domain and leucine-rich repeat protein phosphatase), which regulate AKT activity.
There is limited available information on disease associations specifically linked to AKTIP protein. However, dysregulation of AKT signaling has been implicated in various diseases, such as cancer, diabetes, and neurodegenerative disorders. Since AKTIP is involved in the regulation of AKT signaling, further research is needed to explore if any abnormalities or mutations in AKTIP are associated with specific diseases.
Current knowledge about post-translational modifications of AKTIP protein is limited. However, like many other proteins, it is possible that AKTIP undergoes post-translational modifications such as phosphorylation, acetylation, ubiquitination, or methylation. These modifications can potentially regulate AKTIP's function and interaction with other proteins, but further research is needed to fully understand the post-translational modifications of AKTIP.
Limited studies have investigated the regulation of AKTIP expression. One study found that the transcription factor EGR1 can bind to the promoter region of AKTIP and regulate its expression in certain cancer cells. Another study suggested a role for the microRNA miR-29a in downregulating AKTIP expression in ovarian cancer cells. More research is necessary to fully understand the mechanisms and factors involved in the regulation of AKTIP expression.
Currently, there are no specific diseases or disorders that have been directly linked to AKTIP protein. However, dysregulation of AKT signaling has been implicated in various diseases, including cancer, cardiovascular diseases, neurodegenerative diseases, and metabolic disorders. Since AKTIP interacts with AKT and regulates its activity, it is possible that alterations in AKTIP expression or function could indirectly contribute to the development or progression of these diseases. Further research is needed to explore any potential disease associations with AKTIP.
The primary known functional role of AKTIP protein is its interaction with and regulation of AKT signaling. However, there is evidence suggesting that AKTIP might have additional functional roles. For example, studies have shown that AKTIP is involved in the regulation of cell migration, invasion, and apoptosis. Further research is needed to elucidate the precise mechanisms and additional functional roles of AKTIP.
Customer Reviews (4)
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